USP17L4 Activators

USP17L4, which stands for Ubiquitin-Specific Peptidase 17-Like Family Member 4, is a member of the deubiquitinating enzyme (DUB) family. The USP17 family, to which USP17L4 belongs, is characterized by its ability to cleave ubiquitin moieties from ubiquitinated proteins. This enzymatic process is critical for maintaining the balance of protein ubiquitination, a post-translational modification that typically marks proteins for degradation by the proteasome.The USP17 gene family, including USP17L4, is located on human chromosome 4q13 and includes several homologous genes that appear to have arisen from gene duplication events. These genes encode cysteine proteases that share a common USP domain but differ in their specific substrate affinities and expression patterns. USP17L4, much like its family members, is believed to play a role in the regulation of cellular processes by rescuing proteins from degradation, thereby impacting signal transduction, cell cycle control, and apoptosis.

USP17L4's precise biological functions remain less characterized when compared to other DUBs; however, DUBs are generally implicated in various cellular pathways and have been associated with the pathophysiology of diseases such as cancer, neurodegeneration, and infections. The deubiquitinating activity of USP17L4 potentially regulates the stability and function of key regulatory proteins within these pathways.The expression of USP17L4 and its family members is often induced by cytokines, suggesting a potential role in immune responses. The reversible nature of ubiquitination, mediated by enzymes like USP17L4, allows for dynamic control over protein function and signaling pathways within the cell. By modulating the ubiquitination status of target proteins, USP17L4 can affect a variety of cellular outcomes, including proliferation, differentiation, and stress responses.